TYSY_IIV6
ID TYSY_IIV6 Reviewed; 295 AA.
AC Q9WBI3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable thymidylate synthase 225R;
DE EC=2.1.1.45;
GN ORFNames=IIV6-225R;
OS Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus.
OX NCBI_TaxID=176652;
OH NCBI_TaxID=6997; Acheta domesticus (House cricket).
OH NCBI_TaxID=168631; Chilo suppressalis (Asiatic rice borer moth).
OH NCBI_TaxID=6999; Gryllus bimaculatus (Two-spotted cricket).
OH NCBI_TaxID=58607; Gryllus campestris.
OH NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11448171; DOI=10.1006/viro.2001.0963;
RA Jakob N.J., Mueller K., Bahr U., Darai G.;
RT "Analysis of the first complete DNA sequence of an invertebrate iridovirus:
RT coding strategy of the genome of Chilo iridescent virus.";
RL Virology 286:182-196(2001).
RN [2]
RP GENOME REANNOTATION.
RX PubMed=17239238; DOI=10.1186/1743-422x-4-11;
RA Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.;
RT "Comparative genomic analysis of the family Iridoviridae: re-annotating and
RT defining the core set of iridovirus genes.";
RL Virol. J. 4:11-11(2007).
RN [3]
RP FUNCTION.
RX PubMed=9926400; DOI=10.1023/a:1008017820941;
RA Muller K., Tidona C.A., Bahr U., Darai G.;
RT "Identification of a thymidylate synthase gene within the genome of Chilo
RT iridescent virus.";
RL Virus Genes 17:243-258(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-
CC dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422;
CC EC=2.1.1.45;
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
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DR EMBL; AF303741; AAD21329.1; -; Genomic_DNA.
DR RefSeq; NP_149688.1; NC_003038.1.
DR SMR; Q9WBI3; -.
DR GeneID; 1733097; -.
DR KEGG; vg:1733097; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000001359; Genome.
DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR Gene3D; 3.30.572.10; -; 1.
DR HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR InterPro; IPR045097; Thymidate_synth/dCMP_Mease.
DR InterPro; IPR023451; Thymidate_synth/dCMP_Mease_dom.
DR InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
DR InterPro; IPR000398; Thymidylate_synthase.
DR InterPro; IPR020940; Thymidylate_synthase_AS.
DR PANTHER; PTHR11548; PTHR11548; 1.
DR Pfam; PF00303; Thymidylat_synt; 1.
DR PRINTS; PR00108; THYMDSNTHASE.
DR SUPFAM; SSF55831; SSF55831; 1.
DR TIGRFAMs; TIGR03284; thym_sym; 1.
DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Nucleotide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..295
FT /note="Probable thymidylate synthase 225R"
FT /id="PRO_0000377772"
FT ACT_SITE 167
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 27
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 147..148
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 192..195
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 195
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 203
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 238..240
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 294
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
SQ SEQUENCE 295 AA; 33961 MW; 84E3A627EBF7AF02 CRC64;
MDINNEEKQY LNLLEKVLFQ GEDRDDRTGI GTKNVFGEQL KFNLRTSFPL LTTKKVFWKG
VVEELLWFIS GSTDVSVLNQ KGVKIWNKNA ESFYTQQNLF KKNDLGPIYG FQWRHYGENY
IGCDNKYGGI DQLKNIITTI QNEPWDRRMI LLAWNPKDNS KMALPPCHCI AHFDVSSKIN
GKRELSCHLF QRSADMGLGV PFNIASYALL THIIAHVSST NTELIVPGDF VHTLSNVHIY
KNHIKALTEQ ISRIPRKFPT LEIINKNKNI DAFSSKDFVL KDYNPYPALE MEMAL
